1gn1: Difference between revisions

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|PDB= 1gn1 |SIZE=350|CAPTION= <scene name='initialview01'>1gn1</scene>, resolution 2.80&Aring;
|PDB= 1gn1 |SIZE=350|CAPTION= <scene name='initialview01'>1gn1</scene>, resolution 2.80&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gn1 OCA], [http://www.ebi.ac.uk/pdbsum/1gn1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gn1 RCSB]</span>
}}
}}


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[[Category: Willison, K R.]]
[[Category: Willison, K R.]]
[[Category: Wilsher, J.]]
[[Category: Wilsher, J.]]
[[Category: CA]]
[[Category: actin]]
[[Category: actin]]
[[Category: chaperone]]
[[Category: chaperone]]
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[[Category: tubulin]]
[[Category: tubulin]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:25:14 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:47:17 2008''

Revision as of 20:47, 30 March 2008

File:1gn1.gif


PDB ID 1gn1

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE MOUSE CCT GAMMA APICAL DOMAIN (MONOCLINIC)


OverviewOverview

The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only member of the chaperonin family found in the cytosol of eukaryotes. Like other chaperonins, it assists the folding of newly synthesised proteins. It is, however, unique in its specificity towards only a small subset of non-native proteins. We determined two crystal structures of mouse CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a surface patch facing the inside of the torus that is highly evolutionarily conserved and specific for the CCTgamma apical domain. This putative substrate-binding region consists of predominantly positively charged side-chains. It suggests that the specificity of this apical domain towards its substrate, partially folded tubulin, is conferred by polar and electrostatic interactions. The site and nature of substrate interaction are thus profoundly different between CCT and its eubacterial homologue GroEL, consistent with their different functions in general versus specific protein folding assistance.

About this StructureAbout this Structure

1GN1 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin., Pappenberger G, Wilsher JA, Roe SM, Counsell DJ, Willison KR, Pearl LH, J Mol Biol. 2002 May 17;318(5):1367-79. PMID:12083524

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